期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 114, 期 19, 页码 6707-6712出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp101096r
关键词
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资金
- Natural Sciences and Engineering Research Council of Canada (NSERC)
- NSERC Canada Research Chair in Proteins, Biosystems and Functional Foods
beta-Lactoglobulin (beta-LG), the major whey protein in bovine milk, binds to a wide range of compounds. Folic acid (FA) is a synthetic form of the B group vitamin known as folates, which are essential cofactors for a variety of physiological processes. The interaction of beta-LG with FA was studied using fluorescence spectroscopy to determine the FA binding constant and mode and the influence of the protein on FA photodegradation. At <= 20 mu M FA, which may be the critical self-association concentration, the binding constant and number are 2.0 (+/-0.6) x 10(6) M-1 and 1.30 (+/-0.03) when excited at 280 nm and 4.3 (+/-2.2) x 10(5) M-1 and 1.17 (+/-0.04) at 295 nm, as determined by protein intrinsic fluorescence. FA binds to the surface of beta-LG, possibly in the groove between the alpha-helix and the beta-barrel. Fluorescence analysis of the pterin portion of FA shows that complexation with beta-LG improves FA photostability. It is suggested that beta-LG complexes could be used as an effective carrier of FA in functional foods.
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